Nonenzymic glycation of proteins by glucose and subsequent rearrangement of the Amadori product leads to the formation of what are presently known as Advanced Glycation End Products or AGEs. The formation of AGEs in turn can also lead to the crosslinking of proteins. AGEs represent a family of compounds characterized by yellow-brown pigmentation, and many of them are also highly fluorescent. The structure of only a few AGEs have been characterized to date. The process of AGE formation has been demonstrated to be accelerated in diabetes, but also occurs at a slower rate in everyone. We are interested in identifying and characterizing one or more of the AGEs that are formed as a result of sugar interactions with proteins. The objective of the present study is to identify and characterize new AGE species in biological samples. The AGE species in biological samples will be separated by HPLC analysis and their mass and fragmentation patterns determined with a view to using this data with other physicochemical measurements to aid in the elucidation of the chemical structures of new AGE species.